ID A0A0B0HC33_SOVGS Unreviewed; 776 AA.
AC A0A0B0HC33;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Penicillin-binding protein 1A {ECO:0000256|ARBA:ARBA00018638};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
DE EC=3.4.16.4 {ECO:0000256|ARBA:ARBA00012448};
GN Name=mrcA {ECO:0000313|EMBL:KHF26620.1};
GN ORFNames=BOV88_01380 {ECO:0000313|EMBL:OOY36268.1}, JV46_23660
GN {ECO:0000313|EMBL:KHF26620.1};
OS Solemya velum gill symbiont.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX NCBI_TaxID=2340 {ECO:0000313|EMBL:KHF26620.1, ECO:0000313|Proteomes:UP000030856};
RN [1] {ECO:0000313|EMBL:KHF26620.1, ECO:0000313|Proteomes:UP000030856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH {ECO:0000313|EMBL:KHF26620.1,
RC ECO:0000313|Proteomes:UP000030856};
RX PubMed=25342549; DOI=10.1186/1471-2164-15-924;
RA Dmytrenko O., Russell S.L., Loo W.T., Fontanez K.M., Liao L., Roeselers G.,
RA Sharma R., Stewart F.J., Newton I.L., Woyke T., Wu D., Lang J.M.,
RA Eisen J.A., Cavanaugh C.M.;
RT "The genome of the intracellular bacterium of the coastal bivalve, Solemya
RT velum: a blueprint for thriving in and out of symbiosis.";
RL BMC Genomics 15:924-924(2014).
RN [2] {ECO:0000313|EMBL:OOY36268.1, ECO:0000313|Proteomes:UP000190962}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MA-KB16 {ECO:0000313|EMBL:OOY36268.1};
RA Russell S.L., Corbett-Detig R.B., Cavanaugh C.M.;
RT "Mixed transmission modes and dynamic genome evolution in an obligate
RT animal-bacterial symbiosis.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cell wall formation. Synthesis of cross-linked peptidoglycan
CC from the lipid intermediates. The enzyme has a penicillin-insensitive
CC transglycosylase N-terminal domain (formation of linear glycan strands)
CC and a penicillin-sensitive transpeptidase C-terminal domain (cross-
CC linking of the peptide subunits). {ECO:0000256|ARBA:ARBA00002624}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also
CC transpeptidation of peptidyl-alanyl moieties that are N-acyl
CC substituents of D-alanine.; EC=3.4.16.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034000};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-
CC Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-
CC (1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-
CC cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-
CC D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl
CC diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+);
CC Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602, Rhea:RHEA-COMP:9603,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58405, ChEBI:CHEBI:60033,
CC ChEBI:CHEBI:78435; EC=2.4.1.129;
CC Evidence={ECO:0000256|ARBA:ARBA00023988};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004249}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004249}. Membrane
CC {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the transpeptidase
CC family. {ECO:0000256|ARBA:ARBA00007090}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC glycosyltransferase 51 family. {ECO:0000256|ARBA:ARBA00007739}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KHF26620.1}.
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DR EMBL; JRAA01000001; KHF26620.1; -; Genomic_DNA.
DR EMBL; MPNX01000001; OOY36268.1; -; Genomic_DNA.
DR RefSeq; WP_052132068.1; NZ_MPQZ01000051.1.
DR AlphaFoldDB; A0A0B0HC33; -.
DR STRING; 2340.JV46_23660; -.
DR PATRIC; fig|2340.3.peg.1136; -.
DR eggNOG; COG5009; Bacteria.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000030856; Unassembled WGS sequence.
DR Proteomes; UP000190962; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR Gene3D; 1.10.3810.10; Biosynthetic peptidoglycan transglycosylase-like; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 2.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR001264; Glyco_trans_51.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR031376; PCB_OB.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR NCBIfam; TIGR02074; PBP_1a_fam; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF27; PENICILLIN-BINDING PROTEIN 1A; 1.
DR Pfam; PF17092; PCB_OB; 1.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000030856};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 59..234
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 320..435
FT /note="Penicillin-binding protein OB-like"
FT /evidence="ECO:0000259|Pfam:PF17092"
FT DOMAIN 438..689
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 776 AA; 86164 MW; 93CC6D9E8E508C2F CRC64;
MKSIGQFINF LLAMVMTGGM LVSLGIASAW FYLDSQLPDA EQLRDVRLQI PLRIYSAEGD
MISEYGEKRR EPLTREEIPD AMVKAILAVE DSNFYTHPGV DYKGLLRAAV SLIKTGRKKQ
GGSTITMQLA RNFFLSPEKS YKRKFLEILL ALRVERELEK DEILTLYLNK VYLGHRSYGI
TSAAHTYYNK ELDELSLAEI AMIAGLPKAP SSNNPLTNPE RALKRRNHVL KRMHTLEHIS
DAVYEAETAK PITASRYTPE IELGAAYIGE MVRAEMVERF GDAAYTGGYH VHTTVKTRLQ
RAANKALRTA LDAYDMRHGY RGPETQIVGW QDANERARQL GRLLAVGNLL PVIVVDIPSE
REIVVEHADG SRRTIGWQGL KWASPYVSVN RLGKEPKRAV DIVSLGDLVR IAYVENEKDK
QGELRSYWRL AQIPKAQGAL VSLDPHTGAV IALAGGYDFF HSKFNRVTQA SRQPGSGFKG
FIYSAALAAG FQPSSIINDA PVVIEDVTLD SGVWKPSNAN RKFTGPTPLR QGLAFSKNLI
SIRLLRSISI DFALDHVTRF GFDKDKLPDG LALALGSAEV TPLMMARAYS VFANGGFLVN
PFQIVRIEQE GVGTIYRAKP LRACEVCPAD EQAPRTVSAE NRYLIYSMMK DVINMGTGKD
AKVLGRKDLA GKTGTTNDYK DAWFNGYNES LVAVAWVGLD NSLTLGRREF SGRAALPAWI
DYMRVALDGV PETEPQQPEG IVHNGADFED VTVEAIFNPE VLDVLDEKPQ AEDDLF
//
